Protein antigens of Streptococcus mutans: purification and properties of a double antigen and its protease-resistant component
Protein antigens of Streptococcus mutans: purification and properties of a double antigen and its protease-resistant component
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变形链球菌蛋白抗原：双抗原及其蛋白酶抗性成分的纯化和性质
DOI：
10.1128/iai.28.2.486-493.1980
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发表时间：
1980
影响因子：
3.1
通讯作者：
T. Lehner
中科院分区：
文献类型：
--
作者：
M. Russell;L. Bergmeier;E. Zanders;T. Lehner
具有两组抗原决定簇(抗原I和II)的变形链球菌表面蛋白抗原通过柱层析从变形链球菌血清型c的培养物上清液中纯化。蛋白酶抗性成分，即抗原 II，是从链霉蛋白酶消化的抗原 I/II 中纯化出来的。对抗原进行化学和免疫学分析，并研究其理化特性。抗原I/II由超过80%的蛋白质组成，其肽链分子量估计为185,000。抗原II由大约60%的蛋白质组成，肽链分子量为48,000。在兔子中制备抗原 I/II 和 II 的抗血清，并用于研究其他链球菌细胞中抗原的存在。这表明，不仅c血清型，e和f血清型也具有抗原I和II决定簇，而a、d和g血清型具有与抗原I相关的决定簇，但不具有与抗原II相关的决定簇。
A surface protein antigen of Streptococcus mutans having two sets of antigenic determinants (antigens I and II) was purified by column chromatography from culture supernatants of S. mutans serotype c. The protease-resistant component, antigen II, was purified from pronase-digested antigen I/II. The antigens were analyzed chemically and immunologically, and their physicochemical properties were investigated. Antigen I/II consisted of more than 80% protein, and its peptide chain molecular weight was estimated to be 185,000. Antigen II consisted of approximately 60% protein, with a peptide chain molecular weight of 48,000. Antisera to antigens I/II and II were raised in rabbits and used to investigate the presence of the antigens in cells of other streptococci. This indicated that not only serotype c but also serotypes e and f possessed antigen I and II determinants, whereas serotypes a, d, and g possessed a determinant related to antigen I but not one related to antigen II.